Whole-body protein metabolism and energy expenditure in sheep selected for divergent wool production when fed above or below maintenance

2008 ◽  
Vol 48 (5) ◽  
pp. 657 ◽  
Author(s):  
L. Li ◽  
V. H. Oddy ◽  
J. V. Nolan
Keyword(s):  
Energy Expenditure ◽  
Intravenous Injection ◽  
Protein Metabolism ◽  
Body Tissue ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein ◽  
Wool Production ◽  
Wool Growth

Rates of whole-body protein turnover and energy expenditure were measured in two groups of wethers differing in estimated breeding values (EBVs) for wool growth, but with similar EBVs for fibre diameter and liveweight (LW). The sheep were offered a pelleted diet at 1.2 times their metabolisable energy (ME) requirement for maintenance (1.2 M) followed by either 0.8 M or 1.8 M for 5 weeks. In the 5th week, whole-body protein metabolism was estimated by using intravenous injection of 15N-glycine (g N/day) and whole-body energy expenditure rate (EE) was predicted by the CO2 entry rate technique using intravenous injection of NaH13CO3. The higher N intake (8.7 v. 20.4 g N/day, P < 0.001) was associated with a higher whole-body protein flux (22.1 v. 34.2 g N/day, P < 0.001), and a higher whole-body protein synthesis rate (17.0 v. 25.5 g N/day, P < 0.001) and protein degradation rate (15.9 v. 20.7 g N/day, P < 0.001). Irrespective of feeding levels, sheep with high-fleece EBVs (F+) synthesised and degraded more body protein N (g N/day) than sheep with low-fleece EBVs (F–), and F+ sheep also retained more ingested protein N (P < 0.05) in wool and body tissue than F– sheep, but the significant differences due to genotypes disappeared when whole-body protein flux, synthesis and degradation were expressed as g N/kg LW0.75.day (metabolic weight). Estimates of EE were lower when the sheep were offered 0.8 M than when offered 1.8 M (5.85 v. 7.68 MJ/day, P < 0.001) and were higher in F+ than in F– sheep (6.95 v. 6.58 MJ/day; P < 0.05), but F+ sheep had a significantly lower (P < 0.05) EE (MJ/kg LW0.75.day) than F– sheep. F+ animals also retained more energy in wool and wool-free body tissue than F– animals (P < 0.05). The present study indicates that genetic selection for wool growth has resulted in increased efficiency of dietary protein and energy use for wool production and body-tissue growth in these sheep. Furthermore, there is no ‘trade off’ between deposition of nutrients in the body and wool in sheep with high EBVs for wool growth.

Effect of spaceflight on human protein metabolism

1993 ◽  
Vol 264 (5) ◽  
pp. E824-E828 ◽  
Author(s):  
T. P. Stein ◽  
M. J. Leskiw ◽  
M. D. Schluter
Keyword(s):  
Protein Synthesis ◽  
Nitrogen Balance ◽  
Protein Metabolism ◽  
Space Shuttle ◽  
Single Pulse ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein ◽  
Space Shuttle Columbia

Nitrogen balance and the whole body protein synthesis rate were measured before, during, and after a 9.5-day spaceflight mission on the space shuttle Columbia. Protein synthesis was measured by the single-pulse [15N]glycine method. Determinations were made 56, 26, and 18 days preflight, on flight days 2 and 8, and on days 0, 6, 14, and 45 postflight. We conclude that nitrogen balance was decreased during spaceflight. The decrease in nitrogen balance was greatest on the 1st day when food intake was reduced and again toward the end of the mission. An approximately 30% increase in protein synthesis above the preflight baseline was found for flight day 8 for all 6 subjects (P < 0.05), indicating that the astronauts showed a stress response to spaceflight.

Protein kinetics in stable heart failure patients

2003 ◽  
Vol 94 (1) ◽  
pp. 295-300 ◽  
Author(s):  
Charles W. Cortes ◽  
Paul D. Thompson ◽  
Niall M. Moyna ◽  
Margaret D. Schluter ◽  
Maria J. Leskiw ◽  
...  
Keyword(s):  
Protein Metabolism ◽  
Protein Turnover ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Bed Rest ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein ◽  
Fractional Synthesis

Heart failure (HF) is a slow progressive syndrome characterized by low cardiac output and peripheral metabolic, biochemical, and histological alterations. Protein loss and reduced protein turnover occur with aging, but the consequences of congestive HF (CHF) superimposed on the normal aging response are unknown. This study has two objectives: 1) to determine whether there was a difference between older age-matched controls and those with stable HF (i.e., ischemic pathology) in whole body protein turnover and 2) to determine whether protein metabolism in liver and skeletal muscle protein turnover is impacted by CHF. We measured the whole body protein synthesis rate with a U-15N-labeled algal protein hydrolysate in 10 patients with CHF and in 10 age-matched controls. Muscle fractional synthesis rate of lateral vastus muscle was determined with [U-13C]alanine on muscle biopsies obtained by a standard percutaneous needle biopsy technique. Fractional synthesis rates of five plasma proteins of hepatic origin (fibrinogen, complement C-3, ceruloplasmin, transferrin, and very low-density lipoprotein apoliprotein B-100) were determined by using2H5-labeled l-phenylalanine as tracer. Results showed that whole body protein synthesis rate was reduced in CHF patients (3.09 ± 0.19 vs. 2.25 ± 0.71 g protein · kg−1 · day−1, P < 0.05) as was muscle fractional synthesis rate (3.02 ± 0.58 vs. 1.33 ± 0.71%/day, P < 0.05) and very low-density lipoprotein apoliprotein B-100 (265 ± 25 vs. 197 ± 16%/day, P < 0.05). CHF patients were hyperinsulinemic (9.6 ± 3.1 vs. 47.0 ± 7.8 μU/ml, P < 0.01). The results were compared with those found with bed rest patients. In conclusion, protein turnover is depressed in CHF patients, and both skeletal muscle and liver are impacted. These results are similar to those found with bed rest, which suggests that inactivity is a factor in depressed protein metabolism.

scholarly journals Increased plasma Gln and Leu Raand inappropriately low muscle protein synthesis rate in AIDS wasting

1998 ◽  
Vol 275 (4) ◽  
pp. E577-E583 ◽  
Author(s):  
Kevin E. Yarasheski ◽  
Jeffrey J. Zachwieja ◽  
Jennifer Gischler ◽  
Jan Crowley ◽  
Mary M. Horgan ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Asymptomatic Group ◽  
Body Protein ◽  
Asymptomatic Subjects ◽  
Muscle Protein Synthesis Rate

Muscle protein wasting occurs in human immunodeficiency virus (HIV)-infected individuals and is often the initial indication of acquired immunodeficiency syndrome (AIDS). Little is known about the alterations in muscle protein metabolism that occur with HIV infection. Nine subjects with AIDS wasting (CD4 < 200/mm3), chronic stable opportunistic infections (OI), and ≥10% weight loss, fourteen HIV-infected men and one woman (CD4 > 200/mm3) without wasting or OI (asymptomatic), and six HIV-seronegative lean men (control) received a constant intravenous infusion of [1-13C]leucine (Leu) and [2-15N]glutamine (Gln). Plasma Leu and Gln rate of appearance (Ra), whole body Leu turnover, disposal and oxidation rates, and [13C]Leu incorporation rate into mixed muscle protein were assessed. Total body muscle mass/fat-free mass was greater in controls (53%) than in AIDS wasting (43%; P = 0.04). Fasting whole body proteolysis and synthesis rates were increased above control in the HIV+ asymptomatic group and in the AIDS-wasting group ( P = 0.009). Whole body Leu oxidation rate was greater in the HIV+ asymptomatic group than in the control and AIDS-wasting groups ( P < 0.05). Fasting mixed muscle protein synthesis rate was increased in the asymptomatic subjects (0.048%/h; P = 0.01) but was similar in AIDS-wasting and control subjects (0.035 vs. 0.037%/h). Plasma Gln Rawas increased in AIDS-wasting subjects but was similar in control and HIV+ asymptomatic subjects ( P < 0.001). These findings suggest that AIDS wasting results from 1) a preferential reduction in muscle protein, 2) a failure to sustain an elevated rate of mixed muscle protein synthesis while whole body protein synthesis is increased, and 3) a significant increase in Gln release into the circulation, probably from muscle. Several interesting explanations for the increased Gln Rain AIDS wasting exist.

Whole body protein metabolism and resting energy expenditure in pregnant Gambian women

1992 ◽  
Vol 263 (4) ◽  
pp. E624-E631 ◽  
Author(s):  
L. Willommet ◽  
Y. Schutz ◽  
R. Whitehead ◽  
E. Jequier ◽  
E. B. Fern
Keyword(s):  
Protein Synthesis ◽  
Energy Expenditure ◽  
Protein Metabolism ◽  
Resting Energy Expenditure ◽  
First Trimester ◽  
Significant Rise ◽  
Whole Body ◽  
Body Protein ◽  
Fed State ◽  
Resting Energy

Whole body protein metabolism and resting energy expenditure (REE) were measured at 11, 23, and 33 wk of pregnancy in nine pregnant (not malnourished) Gambian women and in eight matched nonpregnant nonlactating (NPNL) matched controls. Rates of whole body nitrogen flux, protein synthesis, and protein breakdown were determined in the fed state from the level of isotope enrichment of urinary urea and ammonia during a period of 9 h after a single oral dose of [15N]glycine. At regular intervals, REE was measured by indirect calorimetry (hood system). Based on the arithmetic end-product average of values obtained with urea and ammonia, a significant increase in whole body protein synthesis was observed during the second trimester (5.8 +/- 0.4 g.kg-1.day-1) relative to values obtained both for the NPNL controls (4.5 +/- 0.3 g.kg-1.day-1) and those during the first trimester (4.7 +/- 0.3 g.kg-1.day-1). There was a significant rise in REE during the third trimester both in the preprandial and postprandial states. No correlation was found between REE after meal ingestion and the rate of whole body protein synthesis.

Adult Trichostrongylus colubriformis infection did not affect protein synthesis rate in whole-body, intestinal, hepatic and skeletal muscle tissues of lambs fed fresh Lucerne (Medicago sativa)

2007 ◽  
Vol 87 (3) ◽  
pp. 315-325 ◽  
Author(s):  
E. N. Bermingham ◽  
W. C. McNabb ◽  
I. A. Sutherland ◽  
B. R. Sinclair ◽  
B. P. Treloar ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Medicago Sativa ◽  
Parasitic Infection ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Lymphoid Tissues ◽  
Trichostrongylus Colubriformis ◽  
Body Protein

The effects of an established Trichostrongylus colubriformis infection on the whole-body and fractional protein synthesis rates in the small intestine, liver, lymphoid tissues, skeletal muscle and skin were determined in lambs fed fresh Lucerne (Medicago sativa; 800 g DM d-1) on day 48 post-infection. Lambs were dosed with 6000 L3 T. colubriformis larvae for 6 d (n = 5) or kept as parasite-free controls (n = 6). On day 45, the lambs received a bolus injection of deuterated water to measure the size of the whole-body water pool. On day 48, the lambs were continuously infused with [3, 4-3H]-valine into the jugular vein and [1-13C]-valine in the abomasum for 8 h. During the infusion, mesenteric artery blood and terminal tissue samples were collected for measuring the isotopic activity of plasma water, plasma valine, intra cellular valine and protein-bound valine. Intestinal worm numbers on day 48 were higher (P < 0.001) in the infected lambs, however, there was no effect (P > 0.10) of parasitic infection on feed intake, liveweight gain, whole-body protein synthesis and fractional protein synthesis of most tissues. Key words: Parasite infection, protein synthesis, lambs

Whole body and forearm substrate metabolism in hyperthyroidism: evidence of increased basal muscle protein breakdown

2005 ◽  
Vol 288 (6) ◽  
pp. E1067-E1073 ◽  
Author(s):  
Anne Lene Dalkjær Riis ◽  
Jens Otto Lunde Jørgensen ◽  
Signe Gjedde ◽  
Helene Nørrelund ◽  
Anne Grethe Jurik ◽  
...  
Keyword(s):  
Amino Acid ◽  
Muscle Protein ◽  
Clinical Manifestations ◽  
Metabolic Effects ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Protein Breakdown ◽  
Body Protein ◽  
Muscle Protein Breakdown

Thyroid hormones have significant metabolic effects, and muscle wasting and weakness are prominent clinical features of chronic hyperthyroidism. To assess the underlying mechanisms, we examined seven hyperthyroid women with Graves' disease before (Ht) and after (Eut) medical treatment and seven control subjects (Ctr). All subjects underwent a 3-h study in the postabsorptive state. After regional catheterization, protein dynamics of the whole body and of the forearm muscles were measured by amino acid tracer dilution technique using [15N]phenylalanine and [2H4]tyrosine. Before treatment, triiodothyronine was elevated (6.6 nmol/l) and whole body protein breakdown was icreased 40%. The net forearm release of phenylalanine was increased in hyperthyroidism (μg·100 ml−1·min−1): −7.0 ± 1.2 Ht vs. −3.8 ± 0.8 Eut ( P = 0.04), −4.2 ± 0.3 Ctr ( P = 0.048). Muscle protein breakdown, assessed by phenylalanine rate of appearance, was increased (μg·100 ml−1·min−1): 15.5 ± 2.0 Ht vs. 9.6 ± 1.4 Eut ( P = 0.03), 9.9 ± 0.6 Ctr ( P = 0.02). Muscle protein synthesis rate did not differ significantly. Muscle mass and muscle function were decreased 10–20% before treatment. All abnormalities were normalized after therapy. In conclusion, our results show that hyperthyroidism is associated with increased muscle amino acid release resulting from increased muscle protein breakdown. These abnormalities can explain the clinical manifestations of sarcopenia and myopathy.

scholarly journals Modulation of the gut microbiota with antibiotic treatment suppresses whole body urea production in neonatal pigs

2013 ◽  
Vol 304 (3) ◽  
pp. G300-G310 ◽  
Author(s):  
Patrycja Puiman ◽  
Barbara Stoll ◽  
Lars Mølbak ◽  
Adrianus de Bruijn ◽  
Henk Schierbeek ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Gut Microbiota ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Urea Synthesis ◽  
Plasma Urea ◽  
Body Protein ◽  
Neonatal Pigs

We examined whether changes in the gut microbiota induced by clinically relevant interventions would impact the bioavailability of dietary amino acids in neonates. We tested the hypothesis that modulation of the gut microbiota in neonatal pigs receiving no treatment (control), intravenously administered antibiotics, or probiotics affects whole body nitrogen and amino acid turnover. We quantified whole body urea kinetics, threonine fluxes, and threonine disposal into protein, oxidation, and tissue protein synthesis with stable isotope techniques. Compared with controls, antibiotics reduced the number and diversity of bacterial species in the distal small intestine (SI) and colon. Antibiotics decreased plasma urea concentrations via decreased urea synthesis. Antibiotics elevated threonine plasma concentrations and turnover, as well as whole body protein synthesis and proteolysis. Antibiotics decreased protein synthesis rate in the proximal SI and liver but did not affect the distal SI, colon, or muscle. Probiotics induced a bifidogenic microbiota and decreased plasma urea concentrations but did not affect whole body threonine or protein metabolism. Probiotics decreased protein synthesis in the proximal SI but not in other tissues. In conclusion, modulation of the gut microbiota by antibiotics and probiotics reduced hepatic ureagenesis and intestinal protein synthesis, but neither altered whole body net threonine balance. These findings suggest that changes in amino acid and nitrogen metabolism resulting from antibiotic- or probiotic-induced shifts in the microbiota are localized to the gut and liver and have limited impact on whole body growth and anabolism in neonatal piglets.

scholarly journals Effect of dietary tryptophan on muscle, liver and whole-body protein synthesis in weaned piglets: relationship to plasma insulin

1991 ◽  
Vol 66 (3) ◽  
pp. 423-435 ◽  
Author(s):  
N. O. Cortamira ◽  
B. Seve ◽  
Y. Lebreton ◽  
P. Ganier
Keyword(s):  
Protein Synthesis ◽  
Growth Performance ◽  
Plasma Insulin ◽  
Live Weight ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Liver Protein ◽  
Deficient Diet ◽  
Body Protein

Two experiments were carried out with piglets, 3–5 kg live weight, to evaluate the effects of feeding a tryptophan (TRP)-deficient diet for 2 weeks on protein synthesis rates measured in vivo 2 h after a meal. In the first experiment on twenty piglets fed on 250 g protein/kg diets, TRP deficiency (0.77 g/16 g nitrogen) as compared with adequacy (1.17 g/16 g N) significantly decreased feed intake, growth performance and fractional protein synthesis rates (FSR), without variation of RNA in longissimus dorsi (LD) and with parallel increases in RNA in semitendinosus (ST) muscle and liver. In the second experiment thirty-two piglets were tube-fed deficient and adequate diets at the two feeding levels (LF) previously achieved. Both TRP and LF significantly increased growth performance and FSR, but not RNA, in LD and ST muscle, with a trend to a synergy between the two factors (TRP x LF interaction). In another muscle, trapezius (TR), the same interaction was only apparent in RNA content. Among the three muscles it was in LD that FSR was the most responsive to dietary TRP (significant muscle x TRP interaction). In the liver the TRP x LF interaction on FSR and not RNA was the major significant effect, indicating that higher TRP and higher LF were both required to get the maximum protein synthesis rate. At 30 min after a meal the same significant interaction effect was shown on plasma glucose, whilst the higher LF increased plasma insulin with both diets. After a further 30 min the appearance of a similar significant effect of the TRP x LF interaction on plasma insulin resulted from its abatement when the deficient diet had been fed at high LF. These results suggest that dietary TRP deficiency decreased muscle and liver protein synthesis rates in relation to a decrease in the post-prandial release of insulin following a decreased rate of nutrient absorption.

Effect of growth hormone and resistance exercise on muscle growth in young men

1992 ◽  
Vol 262 (3) ◽  
pp. E261-E267 ◽  
Author(s):  
K. E. Yarasheski ◽  
J. A. Campbell ◽  
K. Smith ◽  
M. J. Rennie ◽  
J. O. Holloszy ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Treated Group ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein

The purpose of this study was to determine whether growth hormone (GH) administration enhances the muscle anabolism associated with heavy-resistance exercise. Sixteen men (21-34 yr) were assigned randomly to a resistance training plus GH group (n = 7) or to a resistance training plus placebo group (n = 9). For 12 wk, both groups trained all major muscle groups in an identical fashion while receiving 40 micrograms recombinant human GH.kg-1.day-1 or placebo. Fat-free mass (FFM) and total body water increased (P less than 0.05) in both groups but more (P less than 0.01) in the GH recipients. Whole body protein synthesis rate increased more (P less than 0.03), and whole body protein balance was greater (P = 0.01) in the GH-treated group, but quadriceps muscle protein synthesis rate, torso and limb circumferences, and muscle strength did not increase more in the GH-treated group. In the young men studied, resistance exercise with or without GH resulted in similar increments in muscle size, strength, and muscle protein synthesis, indicating that 1) the larger increase in FFM with GH treatment was probably due to an increase in lean tissue other than skeletal muscle and 2) resistance training supplemented with GH did not further enhance muscle anabolism and function.

Albumin and fibrinogen syntheses increase while muscle protein synthesis decreases in head-injured patients

1997 ◽  
Vol 273 (5) ◽  
pp. E898-E902 ◽  
Author(s):  
Odile Mansoor ◽  
Marc Cayol ◽  
Pierre Gachon ◽  
Yves Boirie ◽  
Pierre Schoeffler ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Albumin Synthesis ◽  
Body Protein ◽  
Head Injured ◽  
Injured Patients

The effect of trauma on protein metabolism was investigated in the whole body, muscle, and liver in severely head-injured patients presenting an acute inflammatory response by comparison to fed control subjects receiving a similar diet. Nonoxidative leucine disposal (an index of whole body protein synthesis) and muscle, albumin, and fibrinogen synthesis were determined by means of a primed, continuous infusion ofl-[1-13C]leucine. Nonoxidative leucine disposal increased by 28% in the patients ( P < 0.02). Fractional muscle protein synthesis rate decreased by 50% ( P < 0.01) after injury. Fractional and absolute fribrinogen synthesis rates were multiplied by two and nine, respectively, after injury ( P< 0.001). Albumin levels were lower in patients (25.2 ± 1.2 g/l, means ± SE) than in controls (33.7 ± 1.2 g/l, P < 0.001). However, fractional albumin synthesis rates were increased by 60% in patients (11.4 ± 1.0%/day) compared with controls (7.3 ± 0.4%/day, P < 0.01). Therefore, 1) head trauma induces opposite and large changes of protein synthesis in muscle and acute-phase hepatic proteins, probably mediated by cytokines, glucocorticoids, and other stress hormones, and 2) in these patients, hypoalbuminemia is not due to a depressed albumin synthesis.

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